BMRB Entry 52143

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52143

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 15N and 13C chemical shift assignments for the D1 domain of the human DEAD-box RNA helicase DDX3X
Deposition date:
2023-09-19
Original release date:
2024-03-18
Authors:
Toyama, Yuki; Shimada, Ichio
Citation:

Citation: Toyama, Yuki; Shimada, Ichio. "NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity"  .

Assembly members:

Assembly members:
entity_1, polymer, 279 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGDEDDWSKPLPPSERLEQE LFSGGNTGINFEKYDDIPVE ATGNNCPPHIESFSDVEMGE IIMGNIELTRYTRPTPVQKH AIPIIKEKRDLMACAQTGSG KTAAFLLPILSQIYSDGPGE ALRAMKENGRYGRRKQYPIS LVLAPTRELAVQIYEEARKF SYRSRVRPCVVYGGADIGQQ IRDLERGCHLLVATPGRLVD MMERGKIGLDFCKYLVLDEA DRMLDMGFEPQIRRIVEQDT MPPKGVRHTMMFSATFPKEI QMLARDFLDEYIFLAVGRV

Data sets:
Data typeCount
13C chemical shifts710
15N chemical shifts223
1H chemical shifts283

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1D1 domain1

Entities:

Entity 1, D1 domain 279 residues - Formula weight is not available

The first two Gly residues were introduced to facilitate the cleavage of N-terminal His-SUMO tag.

1   GLYGLYASPGLUASPASPTRPSERLYSPRO
2   LEUPROPROSERGLUARGLEUGLUGLNGLU
3   LEUPHESERGLYGLYASNTHRGLYILEASN
4   PHEGLULYSTYRASPASPILEPROVALGLU
5   ALATHRGLYASNASNCYSPROPROHISILE
6   GLUSERPHESERASPVALGLUMETGLYGLU
7   ILEILEMETGLYASNILEGLULEUTHRARG
8   TYRTHRARGPROTHRPROVALGLNLYSHIS
9   ALAILEPROILEILELYSGLULYSARGASP
10   LEUMETALACYSALAGLNTHRGLYSERGLY
11   LYSTHRALAALAPHELEULEUPROILELEU
12   SERGLNILETYRSERASPGLYPROGLYGLU
13   ALALEUARGALAMETLYSGLUASNGLYARG
14   TYRGLYARGARGLYSGLNTYRPROILESER
15   LEUVALLEUALAPROTHRARGGLULEUALA
16   VALGLNILETYRGLUGLUALAARGLYSPHE
17   SERTYRARGSERARGVALARGPROCYSVAL
18   VALTYRGLYGLYALAASPILEGLYGLNGLN
19   ILEARGASPLEUGLUARGGLYCYSHISLEU
20   LEUVALALATHRPROGLYARGLEUVALASP
21   METMETGLUARGGLYLYSILEGLYLEUASP
22   PHECYSLYSTYRLEUVALLEUASPGLUALA
23   ASPARGMETLEUASPMETGLYPHEGLUPRO
24   GLNILEARGARGILEVALGLUGLNASPTHR
25   METPROPROLYSGLYVALARGHISTHRMET
26   METPHESERALATHRPHEPROLYSGLUILE
27   GLNMETLEUALAARGASPPHELEUASPGLU
28   TYRILEPHELEUALAVALGLYARGVAL

Samples:

sample_1: D1 domain, [U-2H, 13C, 15N; Iled1-13C1H3; Leud/Valg-13C1H3/12CD3], 1.4 mM; MES 20 mM; sodium chloride 150 mM; DTT 5 mM

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HMCM(CG)CBsample_1isotropicsample_conditions_1
3D HMCM(CGCB)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks